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MICOS complex subunit MIC26 (Apolipoprotein O) (MICOS complex subunit MIC23) (Protein FAM121B)

 MIC26_HUMAN             Reviewed;         198 AA.
Q9BUR5; B2R4K9; Q9H3J9;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
27-SEP-2017, entry version 112.
RecName: Full=MICOS complex subunit MIC26 {ECO:0000303|PubMed:25764979};
AltName: Full=Apolipoprotein O;
AltName: Full=MICOS complex subunit MIC23 {ECO:0000303|PubMed:25781180};
AltName: Full=Protein FAM121B;
Flags: Precursor;
Name=APOO;
Synonyms=FAM121B, MIC23 {ECO:0000303|PubMed:25781180},
MIC26 {ECO:0000303|PubMed:25764979}; ORFNames=My025, UNQ1866/PRO4302;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal brain;
Mao Y.M., Xie Y., Zheng Z.H.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Skin, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND COVALENT
LINKAGE WITH CHONDROITIN SULFATE.
PubMed=16956892; DOI=10.1074/jbc.M510861200;
Lamant M., Smih F., Harmancey R., Philip-Couderc P., Pathak A.,
Roncalli J., Galinier M., Collet X., Massabuau P., Senard J.-M.,
Rouet P.;
"ApoO, a novel apolipoprotein, is an original glycoprotein up-
regulated by diabetes in human heart.";
J. Biol. Chem. 281:36289-36302(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
FUNCTION.
PubMed=24743151; DOI=10.1172/JCI74668;
Turkieh A., Caubere C., Barutaut M., Desmoulin F., Harmancey R.,
Galinier M., Berry M., Dambrin C., Polidori C., Casteilla L.,
Koukoui F., Rouet P., Smih F.;
"Apolipoprotein O is mitochondrial and promotes lipotoxicity in
heart.";
J. Clin. Invest. 124:2277-2286(2014).
[9]
FUNCTION, NOMENCLATURE, IDENTIFICATION IN THE MICOS COMPLEX,
SUBCELLULAR LOCATION, GLYCOSYLATION, AND INTERACTION WITH MINOS1;
APOOL AND IMMT.
PubMed=25764979; DOI=10.1016/j.bbamcr.2015.03.004;
Koob S., Barrera M., Anand R., Reichert A.S.;
"The non-glycosylated isoform of MIC26 is a constituent of the
mammalian MICOS complex and promotes formation of crista junctions.";
Biochim. Biophys. Acta 1853:1551-1563(2015).
[10]
IDENTIFICATION IN THE MICOS COMPLEX.
PubMed=25997101; DOI=10.7554/eLife.06265;
Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
Gygi S.P., Van Vactor D., Harper J.W.;
"QIL1 is a novel mitochondrial protein required for MICOS complex
stability and cristae morphology.";
Elife 4:0-0(2015).
[11]
IDENTIFICATION IN THE MICOS COMPLEX, NOMENCLATURE, INTERACTION WITH
IMMT, AND SUBCELLULAR LOCATION.
PubMed=25781180; DOI=10.1371/journal.pone.0120213;
Ott C., Dorsch E., Fraunholz M., Straub S., Kozjak-Pavlovic V.;
"Detailed analysis of the human mitochondrial contact site complex
indicate a hierarchy of subunits.";
PLoS ONE 10:E0120213-E0120213(2015).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Component of the MICOS complex, a large protein complex
of the mitochondrial inner membrane that plays crucial roles in
the maintenance of crista junctions, inner membrane architecture,
and formation of contact sites to the outer membrane. Plays a
crucial role in crista junction formation and mitochondrial
function (PubMed:25764979). Can promote cardiac lipotoxicity by
enhancing mitochondrial respiration and fatty acid metabolism in
cardiac myoblasts (PubMed:24743151). Promotes cholesterol efflux
from macrophage cells. Detected in HDL, LDL and VLDL. Secreted by
a microsomal triglyceride transfer protein (MTTP)-dependent
mechanism, probably as a VLDL-associated protein that is
subsequently transferred to HDL (PubMed:16956892).
{ECO:0000269|PubMed:16956892, ECO:0000269|PubMed:24743151,
ECO:0000269|PubMed:25764979}.
-!- SUBUNIT: Component of the mitochondrial contact site and cristae
organizing system (MICOS) complex, composed of at least
MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60,
APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under
the names MINOS or MitOS complex. he MICOS complex associates with
mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2
(together described as components of the mitochondrial outer
membrane sorting assembly machinery (SAM) complex) and DNAJC11,
mitochondrial inner membrane protein TMEM11 and with HSPA9
(PubMed:25764979, PubMed:25781180, PubMed:25997101). The MICOS and
SAM complexes together with DNAJC11 are part of a large protein
complex spanning both membranes termed the mitochondrial
intermembrane space bridging (MIB) complex Interacts with
IMMT/MIC60 (PubMed:25764979, PubMed:25781180). Interacts with
MINOS1/MIC10 and APOOL/MIC27 (PubMed:25764979).
{ECO:0000269|PubMed:25764979, ECO:0000269|PubMed:25781180,
ECO:0000269|PubMed:25997101, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:25764979}; Single-pass membrane protein
{ECO:0000255}. Secreted {ECO:0000269|PubMed:16956892,
ECO:0000269|PubMed:25764979}. Mitochondrion
{ECO:0000269|PubMed:25781180}. Golgi apparatus membrane
{ECO:0000269|PubMed:25764979}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:25764979}. Note=Exists in three distinct
forms: a glycosylated and secreted form, an ER/Golgi-resident form
and a non-glycosylated mitochondrial form.
{ECO:0000269|PubMed:25764979}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BUR5-1; Sequence=Displayed;
Name=2;
IsoId=Q9BUR5-2; Sequence=VSP_023333;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined. Up-
regulated in diabetic heart. {ECO:0000269|PubMed:16956892}.
-!- PTM: O-glycosylation; glycosaminoglycan of chondroitin-sulfate
type. {ECO:0000269|PubMed:16956892, ECO:0000269|PubMed:25764979}.
-!- SIMILARITY: Belongs to the apolipoprotein O/MICOS complex subunit
Mic27 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF061264; AAG43139.1; -; mRNA.
EMBL; AY359114; AAQ89472.1; -; mRNA.
EMBL; AK311865; BAG34806.1; -; mRNA.
EMBL; CH471074; EAW99002.1; -; Genomic_DNA.
EMBL; BC002333; AAH02333.1; -; mRNA.
EMBL; BC010102; AAH10102.1; -; mRNA.
EMBL; BC016814; AAH16814.1; -; mRNA.
CCDS; CCDS14208.1; -. [Q9BUR5-1]
RefSeq; NP_077027.1; NM_024122.4. [Q9BUR5-1]
RefSeq; XP_016885326.1; XM_017029837.1. [Q9BUR5-1]
UniGene; Hs.495851; -.
ProteinModelPortal; Q9BUR5; -.
BioGrid; 122556; 5.
CORUM; Q9BUR5; -.
IntAct; Q9BUR5; 1.
STRING; 9606.ENSP00000368528; -.
iPTMnet; Q9BUR5; -.
PhosphoSitePlus; Q9BUR5; -.
BioMuta; APOO; -.
DMDM; 74733244; -.
EPD; Q9BUR5; -.
MaxQB; Q9BUR5; -.
PaxDb; Q9BUR5; -.
PeptideAtlas; Q9BUR5; -.
PRIDE; Q9BUR5; -.
TopDownProteomics; Q9BUR5-1; -. [Q9BUR5-1]
TopDownProteomics; Q9BUR5-2; -. [Q9BUR5-2]
Ensembl; ENST00000379226; ENSP00000368528; ENSG00000184831. [Q9BUR5-1]
GeneID; 79135; -.
KEGG; hsa:79135; -.
UCSC; uc004dax.4; human. [Q9BUR5-1]
CTD; 79135; -.
DisGeNET; 79135; -.
EuPathDB; HostDB:ENSG00000184831.13; -.
GeneCards; APOO; -.
HGNC; HGNC:28727; APOO.
HPA; HPA003187; -.
MIM; 300753; gene.
neXtProt; NX_Q9BUR5; -.
OpenTargets; ENSG00000184831; -.
PharmGKB; PA162376709; -.
eggNOG; KOG4798; Eukaryota.
eggNOG; ENOG4112AZQ; LUCA.
GeneTree; ENSGT00530000063666; -.
HOGENOM; HOG000034011; -.
HOVERGEN; HBG059567; -.
InParanoid; Q9BUR5; -.
OMA; CEPYTNW; -.
OrthoDB; EOG091G0MR4; -.
PhylomeDB; Q9BUR5; -.
TreeFam; TF315313; -.
Reactome; R-HSA-8949613; Cristae formation.
ChiTaRS; APOO; human.
GeneWiki; Apolipoprotein_O; -.
GenomeRNAi; 79135; -.
PRO; PR:Q9BUR5; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000184831; -.
CleanEx; HS_APOO; -.
ExpressionAtlas; Q9BUR5; baseline and differential.
Genevisible; Q9BUR5; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0061617; C:MICOS complex; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
InterPro; IPR019166; MIC26/MIC27.
InterPro; IPR033182; MIC26/MIC27_animal.
PANTHER; PTHR14564; PTHR14564; 1.
Pfam; PF09769; ApoO; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Glycoprotein; Golgi apparatus; HDL; LDL; Lipid transport; Membrane;
Mitochondrion; Mitochondrion inner membrane; Proteoglycan;
Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix; Transport; VLDL.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 198 MICOS complex subunit MIC26.
/FTId=PRO_0000254646.
TRANSMEM 108 128 Helical. {ECO:0000255}.
CARBOHYD 162 162 O-linked (Xyl...) (chondroitin sulfate)
serine. {ECO:0000255}.
VAR_SEQ 80 109 ETYSQTKPKMQSLVQWGLDSYDYLQNAPPG -> TAMTISK
MHLLD (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_023333.
SEQUENCE 198 AA; 22285 MW; BEC99607F54E98E2 CRC64;
MFKVIQRSVG PASLSLLTFK VYAAPKKDSP PKNSVKVDEL SLYSVPEGQS KYVEEARSQL
EESISQLRHY CEPYTTWCQE TYSQTKPKMQ SLVQWGLDSY DYLQNAPPGF FPRLGVIGFA
GLIGLLLARG SKIKKLVYPP GFMGLAASLY YPQQAIVFAQ VSGERLYDWG LRGYIVIEDL
WKENFQKPGN VKNSPGTK


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